Post-translational modifications during lantibiotic biosynthesis

Research output: Contribution to journalReview articlepeer-review


Recent reports have provided the first insights into the mechanisms of the extensive post-translational modifications involved in the biosynthesis of the lantibiotics, a class of peptide antimicrobial agents. These modifications involve dehydration of several serine and threonine residues followed by intramolecular conjugate additions of cysteines, resulting in extensively cross-linked polycyclic structures. Both in vivo and in vitro studies indicate low substrate specificity of the modification machinery, which has been explored for re-engineering of the structures of a number of members. In addition to these developments in understanding their biosynthesis, studies on the mode of action of several lantibiotics have shown a unique mechanism of binding to lipid II, an intermediate in cell wall biosynthesis.

Original languageEnglish (US)
Pages (from-to)498-507
Number of pages10
JournalCurrent Opinion in Chemical Biology
Issue number5
StatePublished - Oct 2004


  • (Z)-2,3-dehydrobutyrine
  • 2,3-dehydroalanine
  • Dha
  • Dhb
  • Lan
  • MeLan
  • lanthionine
  • methyllanthionine

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry


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